Open AccessPurification, crystallization and preliminary X‐ray analysis of the ligand‐binding domain of human lectin‐like oxidized low‐density lipoprotein receptor 1 (LOX‐1)
Author(s) -
Ishigaki Tomoko,
Ohki Izuru,
Oyama Takuji,
Machida Sachiko,
Morikawa Kousuke,
Tate Shinichi
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105012042
Subject(s) - dimer , monomer , ligand (biochemistry) , crystallography , crystallization , chemistry , cysteine , molecule , derivative (finance) , crystal structure , stereochemistry , receptor , biochemistry , organic chemistry , financial economics , economics , enzyme , polymer
Two different fragments of the ligand‐binding domain of LOX‐1, the major receptor for oxidized low‐density lipoprotein (LDL) on endothelial cells, have been crystallized in different forms. One crystal form contains the disulfide‐linked dimer, which is the form of the molecule present on the cell surface; the other contains a monomeric form of the receptor that lacks the cysteine residue necessary to form disulfide‐linked homodimers. The crystal of the monomeric ligand‐binding domain belongs to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 56.79, b = 67.57, c = 79.02 Å. The crystal of the dimeric form belongs to space group C 2, with unit‐cell parameters a = 70.86, b = 49.56, c = 76.73 Å, β = 98.59°. Data for the dimeric form of the LOX‐1 ligand‐binding domain have been collected to 2.4 Å. For the monomeric form of the ligand‐binding domain, native, heavy‐atom derivative and SeMet‐derivative crystals have been obtained; their diffraction data have been measured to 3.0, 2.4 and 1.8 Å resolution, respectively.